Influence of Protein Concentration and Order of Addition on Thermal Stability of β-Lactoglobulin Stabilizedn-Hexadecane Oil-in-Water Emulsions at Neutral pH

Langmuir ◽  
2005 ◽  
Vol 21 (1) ◽  
pp. 134-139 ◽  
Author(s):  
H-J. Kim ◽  
E. A. Decker ◽  
D. J. McClements
Keyword(s):  
Thermal Stability ◽  
Protein Concentration ◽  
Neutral Ph ◽  
Oil In Water ◽  
Β Lactoglobulin ◽  
Thermal Stability Of

scholarly journals The Effects of Salts on the Stability of the Collagen Helix Under Acidic Conditions

1968 ◽  
Vol 21 (4) ◽  
pp. 821 ◽  
Author(s):  
Anne FW oodlock ◽  
BS Harrap
Keyword(s):  
Thermal Stability ◽  
Carboxyl Groups ◽  
Neutral Ph ◽  
Acid Ph ◽  
Helix Stability ◽  
Acidic Conditions ◽  
Anions And Cations ◽  
The Stability ◽  
Thermal Stability Of ◽  
Positively Charged

In the acid pH region, the relative effects of various salts on the thermal stability of the collagen helix are quite different from their effects at neutral pH. The magnitude of the decrease in thermal stability brought about by the salts studied depends mainly on the nature and concentration of the anion and very little on the nature of the cation, whereas at neutral pH the nature of both anions and cations affects the collagen helix stability, the effects of the two ions being roughly additive. The magnitude of the effect of salts at acid pH is much greater than that at neutral pH whereas for a non-ionized denaturant, urea, the magnitudes at both neutral and acid pH are similar. The data are discussed in terms of possible interactions between salts and the positively charged protein with particular consideration of the effects of salts on the pKa of protein carboxyl groups.

scholarly journals Application of Glycation in Regulating the Heat-Induced Nanoparticles of Egg White Protein

Nanomaterials ◽  
2018 ◽  
Vol 8 (11) ◽  
pp. 943 ◽  
Author(s):  
Chenying Wang ◽  
Xidong Ren ◽  
Yujie Su ◽  
Yanjun Yang
Keyword(s):  
Thermal Stability ◽  
Protein Concentration ◽  
Thermal Denaturation ◽  
Negative Charge ◽  
Activity Index ◽  
Stability Index ◽  
Egg White ◽  
Egg White Protein ◽  
Neutral Conditions ◽  
Thermal Stability Of

Due to the poor thermal stability of egg white protein (EWP), important challenges remain regarding preparation of nanoparticles for EWP above the denaturation temperature at neutral conditions. In this study, nanoparticles were fabricated from conjugates of EWP and isomalto-oligosaccharide (IMO) after heating at 90 °C for 30 min. Meanwhile, the effects of protein concentration, temperature, pH, ionic strength and degree of glycation (DG) on the formation of nanoparticles from IMO-EWP were investigated. To further reveal the formation mechanism of the nanoparticles, structures, thermal denaturation properties and surface properties were compared between EWP and IMO-EWP conjugates. Furthermore, the emulsifying activity index (EAI) and the emulsifying stability index (ESI) of nanoparticles were determined. The results indicated that glycation enhanced thermal stability and net surface charge of EWP due to changes in the EWP structure. The thermal aggregation of EWP was inhibited significantly by glycation, and enhanced with a higher degree of glycation. Meanwhile, the nanoparticles (<200 nm in size) were obtained at pH 3.0, 7.0 and 9.0 in the presence of NaCl. The increased thermal stability and surface net negative charge after glycation contributed to the inhibition. The EAI and ESI of nanoparticles were increased nearly 3-fold and 2-fold respectively, as compared to unheated EWP.

scholarly journals Effect of Genetic Polymorphism on the Thermal Stability of β-Lactoglobulin and κ-Casein Mixture

1991 ◽  
Vol 74 (6) ◽  
pp. 1791-1802 ◽  
Author(s):  
Gilbert Idolo Imafidon ◽  
K.F. Ng-Kwai-Hang ◽  
V.R. Harwalkar ◽  
C.-Y. Ma
Keyword(s):  
Thermal Stability ◽  
Genetic Polymorphism ◽  
Β Lactoglobulin ◽  
Thermal Stability Of

Interactions between β-lactoglobulin and dextran sulfate at near neutral pH and their effect on thermal stability

2009 ◽  
Vol 23 (6) ◽  
pp. 1511-1520 ◽  
Author(s):  
Bongkosh Vardhanabhuti ◽  
Umut Yucel ◽  
John N. Coupland ◽  
E. Allen Foegeding
Keyword(s):  
Thermal Stability ◽  
Dextran Sulfate ◽  
Neutral Ph ◽  
Β Lactoglobulin

Enhancing the thermal stability of soy proteins by preheat treatment at lower protein concentration

2020 ◽  
Vol 306 ◽  
pp. 125593 ◽  
Author(s):  
Wuchao Ma ◽  
Tao Wang ◽  
Jiamei Wang ◽  
Di Wu ◽  
Chao Wu ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Protein Concentration ◽  
Soy Proteins ◽  
Preheat Treatment ◽  
Lower Protein ◽  
Thermal Stability Of
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